Recombinant human TNF alpha protein (His tag)

Specifications

Form

Lyophilized

General info

Function

The TNF protein, primarily secreted by macrophages, binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It induces cell death in specific tumor cell lines and acts as a potent pyrogen, causing fever directly or by stimulating interleukin-1 secretion. TNF is implicated in cachexia induction and can stimulate cell proliferation and differentiation under certain conditions. It impairs regulatory T-cells (Treg) function in rheumatoid arthritis patients through FOXP3 dephosphorylation, upregulating protein phosphatase 1 (PP1), which dephosphorylates 'Ser-418' of FOXP3, inactivating FOXP3 and leading to defective Treg cells. TNF is a key mediator of cell death in the anticancer effect of BCG-stimulated neutrophils with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. It induces insulin resistance in adipocytes by inhibiting insulin-induced IRS1 tyrosine phosphorylation and glucose uptake. TNF plays a role in angiogenesis by inducing VEGF production with IL1B and IL6. Additionally, the TNF intracellular domain (ICD) form stimulates IL12 production in dendritic cells. This supplementary information is collated from multiple sources and compiled automatically.

Sequence similarities

Belongs to the tumor necrosis factor family.

Post-translational modifications

The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space.. The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.. O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.. Tumor necrosis factor, soluble form. The soluble form is demyristoylated at Lys-19 and Lys-20 by SIRT6, promoting its secretion.